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Conformation of mucous glycoproteins in aqueous solvents

, : Conformation of mucous glycoproteins in aqueous solvents. Biopolymers 25(8): 1505-1517

Light-scattering techniques have been used to measure the z-average radius of gyration Rg z-average translational diffusion coefficient Dt and weight-average molecular weight Mw of porcine submaxillary mucin (PSM) in solution. PSM isolated at low shear in the presence of protease inhibitors has a Mw about twice as large as a sample prepared without these precautions. The former sample has a Mw of 17 .times. 106 in 0.1 M NaCl, which decreases to 8 .times. 106 in 6 M guanidine hydrochloride (GdnHCl) and then to 2 .times. 106 on addition of 0.1M mercaptoethanol to the 6M GdnHCl solution. The Rg or .**GRAPHIC**. values obtained for PSM in this work superimpose with those of other authors for different mucin glycoproteins, leading to linear log-log relationship to the molecular weight of the protein core. Comparison of these results with those in the literature for denatured proteins suggest that mucins are linear random coils in which the protein core is stiffened by the presence of the oligosacccharide side chains. The length of the oligosaccharides and the nature of the solvent have little effect on the extension of the protein core. This suggests that the stiffness of the protein core is maintained by steric repulsion of the residues at the beginning of the oligosaccharide chains.


PMID: 3742002

DOI: 10.1002/bip.360250809

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